Literature DB >> 14718655

Chalcone isomerase family and fold: no longer unique to plants.

Michael Gensheimer1, Arcady Mushegian.   

Abstract

Chalcone isomerase, an enzyme in the isoflavonoid pathway in plants, catalyzes the cyclization of chalcone into (2S)-naringenin. Chalcone isomerase sequence family and three-dimensional fold appeared to be unique to plants and has been proposed as a plant-specific gene marker. Using sensitive methods of sequence comparison and fold recognition, we have identified genes homologous to chalcone isomerase in all completely sequenced fungi, in slime molds, and in many gammaproteobacteria. The residues directly involved in the enzyme's catalytic function are among the best conserved across species, indicating that the newly discovered homologs are enzymatically active. At the same time, fungal and bacterial species that have chalcone isomerase-like genes tend to lack the orthologs of the upstream enzyme chalcone synthase, suggesting a novel variation of the pathway in these species.

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Year:  2004        PMID: 14718655      PMCID: PMC2286709          DOI: 10.1110/ps.03395404

Source DB:  PubMed          Journal:  Protein Sci        ISSN: 0961-8368            Impact factor:   6.725


  24 in total

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Authors: 
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Review 10.  Phenylpropanoid biosynthesis and its regulation.

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  17 in total

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Journal:  Plant Cell Rep       Date:  2010-11-03       Impact factor: 4.570

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Review 5.  The Research Progress of Chalcone Isomerase (CHI) in Plants.

Authors:  Yan-Chao Yin; Xiao-Dong Zhang; Zhi-Qiang Gao; Ting Hu; Ying Liu
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7.  Structure, expression profile and phylogenetic inference of chalcone isomerase-like genes from the narrow-leafed lupin (Lupinus angustifolius L.) genome.

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8.  Evolution of the chalcone-isomerase fold from fatty-acid binding to stereospecific catalysis.

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Review 9.  Structure and function of enzymes involved in the biosynthesis of phenylpropanoids.

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